<P>Bacteriorhodopsin (bR) is a light-driven proton pump and a model membrane transport protein. We used time-resolved serial femtosecond crystallography at an x-ray free electron laser to visualize conformational changes in bR from nanoseconds t...
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https://www.riss.kr/link?id=A107643093
Nango, Eriko ; Royant, Antoine ; Kubo, Minoru ; Nakane, Takanori ; Wickstrand, Cecilia ; Kimura, Tetsunari ; Tanaka, Tomoyuki ; Tono, Kensuke ; Song, Changyong ; Tanaka, Rie ; Arima, Toshi ; Yamashita, Ayumi ; Kobayashi, Jun ; Hosaka, Toshiaki ; Mizohata, Eiichi ; Nogly, Przemyslaw ; Sugahara, Michihiro ; Nam, Daewoong ; Nomura, Takashi ; Shimamura, Tatsuro ; Im, Dohyun ; Fujiwara, Takaaki ; Yamanaka, Yasuaki ; Jeon, Byeonghyun ; Nishizawa, Tomohiro ; Oda, Kazumasa ; Fukuda, Masahiro ; Andersson, Rebecka ; Bå ; th, Petra ; Dods, Robert ; Davidsson, Jan ; Matsuoka, Shigeru ; Kawatake, Satoshi ; Murata, Michio ; Nureki, Osamu ; Owada, Shigeki ; Kameshima, Takashi ; Hatsui, Takaki ; Joti, Yasumasa ; Schertler, Gebhard ; Yabashi, Makina ; Bondar, Ana-Nicoleta ; Standfuss, Jö ; rg ; Neutze, Richard ; Iwata, So
2016
-
SCI,SCIE,SCOPUS
학술저널
1552-1557(6쪽)
0
상세조회0
다운로드다국어 초록 (Multilingual Abstract)
<P>Bacteriorhodopsin (bR) is a light-driven proton pump and a model membrane transport protein. We used time-resolved serial femtosecond crystallography at an x-ray free electron laser to visualize conformational changes in bR from nanoseconds t...
<P>Bacteriorhodopsin (bR) is a light-driven proton pump and a model membrane transport protein. We used time-resolved serial femtosecond crystallography at an x-ray free electron laser to visualize conformational changes in bR from nanoseconds to milliseconds following photoactivation. An initially twisted retinal chromophore displaces a conserved tryptophan residue of transmembrane helix F on the cytoplasmic side of the protein while dislodging a key water molecule on the extracellular side. The resulting cascade of structural changes throughout the protein shows how motions are choreographed as bR transports protons uphill against a transmembrane concentration gradient.</P>